Structure of PDB 1buv Chain M Binding Site BS04

Receptor Information
>1buv Chain M (length=174) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
IQGLKWQHNEITFCIQNYTPKVGEYATYEAIRKAFRVWESATPLRFREVP
YAYIREGHEKQADIMIFFAEGFHGDSTPFDGEGGFLAHAYFPGPNIGGDT
HFDSAEPWTVRNEDLNGNDIFLVAVHELGHALGLEHSSDPSAIMAPFYQW
MDTENFVLPDDDRRGIQQLYGGES
Ligand information
Ligand IDCA
InChIInChI=1S/Ca/q+2
InChIKeyBHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Ca+2]
FormulaCa
NameCALCIUM ION
ChEMBL
DrugBankDB14577
ZINC
PDB chain1buv Chain M Residue 1188 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1buv Crystal structure of the complex formed by the membrane type 1-matrix metalloproteinase with the tissue inhibitor of metalloproteinases-2, the soluble progelatinase A receptor.
Resolution2.75 Å
Binding residue
(original residue number in PDB)		D193 G194 G196 F198 D216 E219
Binding residue
(residue number reindexed from 1)		D80 G81 G83 F85 D103 E106
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) H239 H243 H249
Catalytic site (residue number reindexed from 1) H126 H130 H136
Enzyme Commision number 3.4.24.80: membrane-type matrix metalloproteinase-1.
Gene Ontology
Molecular Function
GO:0004222 metalloendopeptidase activity
GO:0008237 metallopeptidase activity
GO:0008270 zinc ion binding
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0031012 extracellular matrix

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Molecular Function
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Cellular Component
External links
PDB RCSB:1buv, PDBe:1buv, PDBj:1buv
PDBsum1buv
PubMed9724659
UniProtP50281|MMP14_HUMAN Matrix metalloproteinase-14 (Gene Name=MMP14)

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